ID   LLDP_ECOL6              Reviewed;         551 AA.
AC   P65253; Q8XDF9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=L-lactate permease {ECO:0000250|UniProtKB:P33231};
GN   Name=lldP; Synonyms=lctP; OrderedLocusNames=c4425;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Uptake of L-lactate across the membrane (By similarity). Can
CC       also transport D-lactate and glycolate (By similarity). Seems to be
CC       driven by a proton motive force (By similarity).
CC       {ECO:0000250|UniProtKB:P33231}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out);
CC         Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651;
CC         Evidence={ECO:0000250|UniProtKB:P33231};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29417;
CC         Evidence={ECO:0000250|UniProtKB:P33231};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lactate(in) + H(+)(in) = (R)-lactate(out) + H(+)(out);
CC         Xref=Rhea:RHEA:71791, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004;
CC         Evidence={ECO:0000250|UniProtKB:P33231};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71793;
CC         Evidence={ECO:0000250|UniProtKB:P33231};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycolate(in) + H(+)(in) = glycolate(out) + H(+)(out);
CC         Xref=Rhea:RHEA:29411, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805;
CC         Evidence={ECO:0000250|UniProtKB:P33231};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29413;
CC         Evidence={ECO:0000250|UniProtKB:P33231};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P33231}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the lactate permease family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN82861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN82861.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001297977.1; NC_004431.1.
DR   AlphaFoldDB; P65253; -.
DR   STRING; 199310.c4425; -.
DR   EnsemblBacteria; AAN82861; AAN82861; c4425.
DR   GeneID; 66672499; -.
DR   KEGG; ecc:c4425; -.
DR   eggNOG; COG1620; Bacteria.
DR   HOGENOM; CLU_021628_0_0_6; -.
DR   OMA; LFVYKMP; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR003804; Lactate_perm.
DR   PANTHER; PTHR30003; PTHR30003; 1.
DR   Pfam; PF02652; Lactate_perm; 1.
DR   TIGRFAMs; TIGR00795; lctP; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..551
FT                   /note="L-lactate permease"
FT                   /id="PRO_0000210375"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        494..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   551 AA;  59186 MW;  086A907410E2027B CRC64;
     MNLWQQNYDP AGNIWLSSLI ASLPILFFFF ALIKLKLKGY VAASWTVAIA LAVALLFYKM
     PVANALASVV YGFFYGLWPI AWIIIAAVFV YKISVKTGQF DIIRSSILSI TPDQRLQMLI
     VGFCFGAFLE GAAGFGAPVA ITAALLVGLG FKPLYAAGLC LIVNTAPVAF GAMGIPILVA
     GQVTGIDSFE IGQMVGRQLP FMTIIVLFWI MAIMDGWRGI KETWPAVVVA GGSFAIAQYL
     SSNFIGPELP DIISSLVSLL CLTLFLKRWQ PVRVFRFGDL GASQVDMTLA HTGYTAGQVL
     RAWTPFLFLT ATVTLWSIPP FKALFASGGA LYEWVINIPV PYLDKLVARM PPVVSEATAY
     AAVFKFDWFS ATGTAILFAA LLSIVWLKMK PSDAISTFGS TLKELALPIY SIGMVLAFAF
     ISNYSGLSST LALALAHTGH AFTFFSPFLG WLGVFLTGSD TSSNALFAAL QATAAQQIGV
     SDLLLVAANT TGGVTGKMIS PQSIAIACAA VGLVGKESDL FRFTVKHSLI FTCMVGVITT
     LQAYVLTWMI P